Structure-based engineering of substrate specificity for pinoresinol-lariciresinol reductases

Pinoresinol–lariciresinol reductases (PLRs) are enzymes involved in the lignan biosynthesis. Here, crystal structures of three PLRs in the apo, substrate-bound and product-bound states, and accompanying mutagenesis provide insight into PLRs catalytic mechanism and suggest a strategy for PLR engineer...

Full description

Bibliographic Details
Main Authors: Ying Xiao, Kai Shao, Jingwen Zhou, Lian Wang, Xueqi Ma, Di Wu, Yingbo Yang, Junfeng Chen, Jingxian Feng, Shi Qiu, Zongyou Lv, Lei Zhang, Peng Zhang, Wansheng Chen
Format: Article
Language:English
Published: Nature Publishing Group 2021-05-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-23095-y
id doaj-c447762f36564f00bfa424a474de6a37
record_format Article
spelling doaj-c447762f36564f00bfa424a474de6a372021-05-16T11:09:46ZengNature Publishing GroupNature Communications2041-17232021-05-0112111110.1038/s41467-021-23095-yStructure-based engineering of substrate specificity for pinoresinol-lariciresinol reductasesYing Xiao0Kai Shao1Jingwen Zhou2Lian Wang3Xueqi Ma4Di Wu5Yingbo Yang6Junfeng Chen7Jingxian Feng8Shi Qiu9Zongyou Lv10Lei Zhang11Peng Zhang12Wansheng Chen13Research and Development Center of Chinese Medicine Resources and Biotechnology, Institute of Chinese Materia Medica, Shanghai University of Traditional Chinese MedicineNational Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of SciencesNational Engineering Laboratory for Cereal Fermentation Technology and School of Biotechnology, Jiangnan UniversityNational Engineering Laboratory for Cereal Fermentation Technology and School of Biotechnology, Jiangnan UniversityResearch and Development Center of Chinese Medicine Resources and Biotechnology, Institute of Chinese Materia Medica, Shanghai University of Traditional Chinese MedicineNational Engineering Laboratory for Cereal Fermentation Technology and School of Biotechnology, Jiangnan UniversityResearch and Development Center of Chinese Medicine Resources and Biotechnology, Institute of Chinese Materia Medica, Shanghai University of Traditional Chinese MedicineResearch and Development Center of Chinese Medicine Resources and Biotechnology, Institute of Chinese Materia Medica, Shanghai University of Traditional Chinese MedicineResearch and Development Center of Chinese Medicine Resources and Biotechnology, Institute of Chinese Materia Medica, Shanghai University of Traditional Chinese MedicineResearch and Development Center of Chinese Medicine Resources and Biotechnology, Institute of Chinese Materia Medica, Shanghai University of Traditional Chinese MedicineResearch and Development Center of Chinese Medicine Resources and Biotechnology, Institute of Chinese Materia Medica, Shanghai University of Traditional Chinese MedicineDepartment of Pharmaceutical Botany, School of Pharmacy, Naval Medical University (Second Military Medical University)National Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of SciencesResearch and Development Center of Chinese Medicine Resources and Biotechnology, Institute of Chinese Materia Medica, Shanghai University of Traditional Chinese MedicinePinoresinol–lariciresinol reductases (PLRs) are enzymes involved in the lignan biosynthesis. Here, crystal structures of three PLRs in the apo, substrate-bound and product-bound states, and accompanying mutagenesis provide insight into PLRs catalytic mechanism and suggest a strategy for PLR engineering.https://doi.org/10.1038/s41467-021-23095-y
collection DOAJ
language English
format Article
sources DOAJ
author Ying Xiao
Kai Shao
Jingwen Zhou
Lian Wang
Xueqi Ma
Di Wu
Yingbo Yang
Junfeng Chen
Jingxian Feng
Shi Qiu
Zongyou Lv
Lei Zhang
Peng Zhang
Wansheng Chen
spellingShingle Ying Xiao
Kai Shao
Jingwen Zhou
Lian Wang
Xueqi Ma
Di Wu
Yingbo Yang
Junfeng Chen
Jingxian Feng
Shi Qiu
Zongyou Lv
Lei Zhang
Peng Zhang
Wansheng Chen
Structure-based engineering of substrate specificity for pinoresinol-lariciresinol reductases
Nature Communications
author_facet Ying Xiao
Kai Shao
Jingwen Zhou
Lian Wang
Xueqi Ma
Di Wu
Yingbo Yang
Junfeng Chen
Jingxian Feng
Shi Qiu
Zongyou Lv
Lei Zhang
Peng Zhang
Wansheng Chen
author_sort Ying Xiao
title Structure-based engineering of substrate specificity for pinoresinol-lariciresinol reductases
title_short Structure-based engineering of substrate specificity for pinoresinol-lariciresinol reductases
title_full Structure-based engineering of substrate specificity for pinoresinol-lariciresinol reductases
title_fullStr Structure-based engineering of substrate specificity for pinoresinol-lariciresinol reductases
title_full_unstemmed Structure-based engineering of substrate specificity for pinoresinol-lariciresinol reductases
title_sort structure-based engineering of substrate specificity for pinoresinol-lariciresinol reductases
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-05-01
description Pinoresinol–lariciresinol reductases (PLRs) are enzymes involved in the lignan biosynthesis. Here, crystal structures of three PLRs in the apo, substrate-bound and product-bound states, and accompanying mutagenesis provide insight into PLRs catalytic mechanism and suggest a strategy for PLR engineering.
url https://doi.org/10.1038/s41467-021-23095-y
work_keys_str_mv AT yingxiao structurebasedengineeringofsubstratespecificityforpinoresinollariciresinolreductases
AT kaishao structurebasedengineeringofsubstratespecificityforpinoresinollariciresinolreductases
AT jingwenzhou structurebasedengineeringofsubstratespecificityforpinoresinollariciresinolreductases
AT lianwang structurebasedengineeringofsubstratespecificityforpinoresinollariciresinolreductases
AT xueqima structurebasedengineeringofsubstratespecificityforpinoresinollariciresinolreductases
AT diwu structurebasedengineeringofsubstratespecificityforpinoresinollariciresinolreductases
AT yingboyang structurebasedengineeringofsubstratespecificityforpinoresinollariciresinolreductases
AT junfengchen structurebasedengineeringofsubstratespecificityforpinoresinollariciresinolreductases
AT jingxianfeng structurebasedengineeringofsubstratespecificityforpinoresinollariciresinolreductases
AT shiqiu structurebasedengineeringofsubstratespecificityforpinoresinollariciresinolreductases
AT zongyoulv structurebasedengineeringofsubstratespecificityforpinoresinollariciresinolreductases
AT leizhang structurebasedengineeringofsubstratespecificityforpinoresinollariciresinolreductases
AT pengzhang structurebasedengineeringofsubstratespecificityforpinoresinollariciresinolreductases
AT wanshengchen structurebasedengineeringofsubstratespecificityforpinoresinollariciresinolreductases
_version_ 1721439851010588672